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Temperature-derivative spectroscopy: a tool for protein dynamics.

J Berendzen·D Braunstein
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Abstract

A relaxation method that measures the derivative of a population with respect to temperature is introduced and used to study the recombination of CO to sperm whale myoglobin after a photolyzing flash. Measurement of the geminate process in the infrared CO-stretch bands shows distributed activation enthalpies with different distributions for each band, transitions between two bands that correspond to photolyzed ligands, and kinetic hole burning. The data are well described by gaussian enthalpy distributions; the results match and complement those of isothermal methods. The temperature-derivative technique is further used to explore the recombination of CO from outside the heme pocket.

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KineticsProtein ConformationProteinsSpectrum AnalysisThermodynamicsJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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BibTeXRIS

J Berendzen, D Braunstein. 1990. Temperature-derivative spectroscopy: a tool for protein dynamics.. https://doi.org/10.1073/pnas.87.1.1

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